| Literature DB >> 3996594 |
P Böhlen, F Esch, A Baird, K L Jones, D Gospodarowicz.
Abstract
Fibroblast growth factor (FGF) has been purified to homogeneity from human brain by a procedure involving salt precipitation, cation-exchange chromatography, Heparin-Sepharose affinity chromatography and reverse-phase HPLC. Isolation was monitored by radioimmunoassay and/or by testing column fractions for their capacity to stimulate the proliferation of vascular endothelial cells in vitro. The amino-terminal sequence of human brain FGF was determined as Pro-Ala-Leu-Pro-Glu-Asp-Gly-Gly-Ser-Gly-Ala-Phe-Pro-. This sequence is identical to that of the amino-terminal region of bovine FGF. Additional evidence, including amino acid composition, chromatographic retention behavior, and immunoreactivity suggest that the human and bovine mitogens are very similar in structure.Entities:
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Year: 1985 PMID: 3996594 DOI: 10.1016/0014-5793(85)80765-1
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124